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Oxidative stress and increased type-IV collagenase levels in bronchoalveolar lavage fluid from newborn babies

Schock, Bettina C., Sweet, David G., Ennis, Madeleine, Warner, Jane A., Young, Ian S. and Halliday, Henry L. (2001) Oxidative stress and increased type-IV collagenase levels in bronchoalveolar lavage fluid from newborn babies Pediatric Research, 50, (1), pp. 29-33. (doi:10.1203/00006450-200107000-00008).

Record type: Article

Abstract

Oxidative stress may increase lung permeability by up-regulation of matrix-metalloproteinase-9 (MMP-9), a type-IV collagenase that can disrupt alveolar basement membranes. We have compared a marker of oxidative stress (protein carbonyl residues) with levels of MMP-9 and its inhibitor, tissue inhibitor of metalloproteinase-1 (TIMP-1), in bronchoalveolar lavage samples from newborn babies. Bronchoalveolar lavage samples (n = 87, two from each time point) were taken in the first 6 postnatal days from 41 ventilated babies: 18 of <29 wk gestation, 10 of 29-36 wk, 9 term with persistent fetal circulation, and 4 term without lung disease. Respiratory disease severity at the time of bronchoalveolar lavage was assessed using the arterial-alveolar oxygen tension ratio. One sample from each time point was used for the measurement of MMP-9 by zymography and TIMP-1 by ELISA. The second sample was used to measure carbonyl group concentrations, also using an ELISA. Correlations were calculated between protein carbonyls, arterial-alveolar oxygen tension ratio, and MMP-9 and TIMP-1 concentrations. Significant correlations were found between carbonyl concentrations and arterial-alveolar oxygen tension ratio (r = 1 -0.325, p = 0.0031, n = 81), MMP-9 (r = 0.331, p < 0.0029, n = 79), and TIMP-1 (r = 0.436, p < 0.0001, n = 87). Worsening respiratory disease in newborn babies is associated with increased carbonyl concentrations in neonatal bronchoal-veolar lavage fluid, and these correlated with MMP-9 and TIMP-1 levels. Increased oxidative stress may damage the lung by increasing type-IV collagenase activity, causing disruption of the extracellular matrix.

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Published date: July 2001

Identifiers

Local EPrints ID: 45462
URI: http://eprints.soton.ac.uk/id/eprint/45462
ISSN: 0031-3998
PURE UUID: 77d14caf-e1ed-47a1-b072-41a2bb4be77b

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Date deposited: 30 Mar 2007
Last modified: 17 Jul 2017 15:12

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Contributors

Author: Bettina C. Schock
Author: David G. Sweet
Author: Madeleine Ennis
Author: Jane A. Warner
Author: Ian S. Young
Author: Henry L. Halliday

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